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Clostridium perfringens
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==== Sialidase ==== [[Neuraminidase|Sialidases]], also called neuraminidases, function to breakdown mucin by [[Hydrolysis|hydrolyzing]] the terminal sialic acid residues located within the protein through the process of [[Desilylation|desialylation]]. ''C. perfringens'' has three sialidases belonging to [[Glycoside hydrolase family 33|glycoside hydrolase family 33 (GH33)]]: NanH, NanI, and NanJ. All strains of ''C. perfringens'' encode for at least one of these enzymes.<ref name=":022" /><ref>{{Cite journal |last1=Medley |first1=Brendon J. |last2=Low |first2=Kristin E. |last3=Irungu |first3=Jackline D. W. |last4=Kipchumba |first4=Linus |last5=Daneshgar |first5=Parandis |last6=Liu |first6=Lin |last7=Garber |first7=Jolene M. |last8=Klassen |first8=Leeann |last9=Inglis |first9=G. Douglas |last10=Boons |first10=Geert-Jan |last11=Zandberg |first11=Wesley F. |last12=Abbott |first12=D. Wade |last13=Boraston |first13=Alisdair B. |date=2024-10-01 |title=A "terminal" case of glycan catabolism: Structural and enzymatic characterization of the sialidases of Clostridium perfringens |journal=Journal of Biological Chemistry |volume=300 |issue=10 |pages=107750 |doi=10.1016/j.jbc.2024.107750 |doi-access=free |pmid=39251137 |pmc=11525138 |bibcode=2024JBiCh.300j7750M |issn=0021-9258}}</ref> ''C. perfringens'' can secrete NanI and NanJ through secretion signal [[peptide]]s located on each protein. Research suggests that NanH operates in the cytoplasm of ''C. perfringens'', as it does not contain a secretion signal peptide. NanH contains only a catalytic domain, whereas NanI and NanJ contain a [[catalytic domain]] and additional [[carbohydrate-binding module]]s (CBMs) to aid in catalytic activity. Located on their N-terminals, NanI contains CBM40, whereas NanJ contains both CBM40 and CBM32. Based on studies analyzing the three-dimensional structure of NanI, its [[active site]] has a pocket-like orientation that aids in the removal of sialic acid residues from sialomucins in the intestinal mucosa.<ref name=":022" />
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